Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

🖤 MT6310 > [lab] proteins > Flashcards

[lab] proteins Flashcards

1
Q

most abundant biomolecule in all cells

A

protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

binds amino acids to another amino acid, forming proteins

A

peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

nonpolar aliphatic r groups

A

GAVLIPM

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

aromatic r group

A

WYF

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

positively charged group

A

RHK

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

negatively charged r group

A

ED

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

polar uncharged group

A

SCTNQ

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

sequence of amino acid residues that serves as the backbone of a peptide chain or protein

A

primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

regular, repeating folding patterns

A

secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

a-helix and b-pleated sheets

A

secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

rod-like structure; h-bonds parallel to axis

A

a-helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

typically amphiphilic

A

a-helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

polypeptide chains arranged side by side; h bonds between chain

A

b-pleated sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

may be parallel or antiparallel

A

b-pleated sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

more stable b-pleated sheets

A

antiparallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

protein fold in 3 dimensions; overall folding of domains

A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

specific overall shape of a protein

A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

cross links between r groups of amino acid in chain

A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

interaction between different polypeptide chains to produce an oligometric structure

A

quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

aggregates of two or more protein chains connected by weak non-covalent interactions

A

quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

proteins with two or more chains

A

quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

classification of proteins

A

(CBSS)
according to composition
according to biological function
according to shape
according to solubility

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

yield only amino acids upon hydrolysis

A

simple proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

simple proteins + non-protein substances

A

conjugated proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
biological functions of proteins
(NETSCDR) nutrient & storage enzymes transport structural contractile & motile defense regulatory
26
polypeptide chain/s folded into spherical /globular shape
globular proteins
27
soluble in aqueous system
globular proteins
28
polypeptide chains arranged in long strands or sheets
fibrous proteins
29
water insoluble protein
fibrous proteins
30
protein classification according to solubility
(AGPAG) albumin globulin prolamin albuminoids/scleroproteins glutelin
31
protein soluble in water and dilute aqueous solutions
albumin (plasma)
32
protein soluble in salt and dilute solutions; insoluble in water
globulins (serum)
33
protein soluble in dilute solutions of acids and bases; insoluble in neutral solvents
glutelins (flour)
34
store protein in plants; soluble in 50-90% alcohol; insoluble in water, neutral solvents, or absolute alcohol
prolamins
35
insoluble in most ordinary solvents
albuminoids/scleroproteins
36
loss of three dimensional structure sufficient to cause of loss of function
protein denaturation
37
leads to primary structure
denaturation
38
leads to destruction of all structure
hydrolysis
39
denaturing agents
(SHARBOTD) salts heavy metals acid (strong) reducing agents base (strong) organic solvent temperature detergents
40
types of denaturation
irreversible & reversible
41
uses strong acid / base + high temperature; product: amino acid
complete hydrolysis
42
uses enzymes called protease; product: mixture of amino acids and oligopeptides
incomplete / partial hydrolysis
43
most commonly used reagent for acid hydrolysis
6N HCl
44
reagent for alkaline hydrolysis
NaOH or KOH
45
partially destroyed amino acid in acid hydrolysis
CY
46
completely destroyed amino acid in acid hydrolysis
W
47
incompletely liberated amino acid in acid hydrolysis
VI
48
racemized and destroyed amino acid in acid hydrolysis
ST
49
in acid hydrolysis N+Q is converted into
D+E
50
advantage of alkaline hydrolysis
W not destroyed
51
disadvantage of alkaline hydrolysis
RNQS are destroyed
52
___ are needed to facilitate the hydrolysis of peptide bonds
catalysts
53
enzymes that hydrolyze peptide binds at specific sites
protease
54
advantage of incomplete / partial hydrolysis
amino acids are not affected
55
presence of proteolytic enzymes result to partial / selective hydrolysis of polypeptide to yield a mixture of peptide fragments
enzymatic hydrolysis
56
requires certain temperature and ph conditions for optimum activity of enzymes
incomplete / partial hydrolysis
57
exopeptidases
carboxypeptidase a carboxypeptidase b aminopeptidase
58
c-terminal residues
carboxypeptidases
59
n-terminal residues
aminopeptidases
60
carboxypeptidase a
c-terminal residues except R,K,P
61
carboxypeptidase b
except R or K at C-terminus
62
aminopeptidase
most n-terminal except when p is the next residue
63
endopeptidases
trypsin chymotrypain papain
64
trypsin
c side R K
65
chymotrypsin
c side W Y F
66
papain
c side of hydrophobic / aromatic r groups
67
properties of proteins to consider in separation / purification of proteins
(CASIM) charge affinity to ligand solubility isoelectric point molecular size/shape
68
procedure in which the ph of the protein mixture is adjusted to the pI of the protein to be isolated to selectively minimize its solubility
isoelectric precipitation
69
change in ionic strength
salting in / salting out
70
relationship of salt concentration and solubility
inverse (high salt conc. = low solubility; vice versa)

🖤 MT6310 (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions